ID   AROQ_AFIC5              Reviewed;         151 AA.
AC   B6JHG1; F8BW39;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00169};
DE            Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00169};
DE            EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00169};
DE   AltName: Full=Type II DHQase {ECO:0000255|HAMAP-Rule:MF_00169};
GN   Name=aroQ {ECO:0000255|HAMAP-Rule:MF_00169};
GN   OrderedLocusNames=OCAR_5981, OCA5_c20430;
OS   Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
OS   (Oligotropha carboxidovorans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Afipia.
OX   NCBI_TaxID=504832;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX   PubMed=18539730; DOI=10.1128/jb.00614-08;
RA   Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.;
RT   "Genome sequence of the chemolithoautotrophic bacterium Oligotropha
RT   carboxidovorans OM5T.";
RL   J. Bacteriol. 190:5531-5532(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX   PubMed=21742883; DOI=10.1128/jb.05619-11;
RA   Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA   Meyer O.;
RT   "Complete genome sequences of the chemolithoautotrophic Oligotropha
RT   carboxidovorans strains OM4 and OM5.";
RL   J. Bacteriol. 193:5043-5043(2011).
CC   -!- FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate.
CC       {ECO:0000255|HAMAP-Rule:MF_00169}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC         Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00169};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       3/7. {ECO:0000255|HAMAP-Rule:MF_00169}.
CC   -!- SUBUNIT: Homododecamer. {ECO:0000255|HAMAP-Rule:MF_00169}.
CC   -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00169}.
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DR   EMBL; CP001196; ACI93101.1; -; Genomic_DNA.
DR   EMBL; CP002826; AEI06750.1; -; Genomic_DNA.
DR   RefSeq; WP_012563128.1; NC_015684.1.
DR   AlphaFoldDB; B6JHG1; -.
DR   SMR; B6JHG1; -.
DR   STRING; 504832.OCAR_5981; -.
DR   EnsemblBacteria; AEI06750; AEI06750; OCA5_c20430.
DR   KEGG; oca:OCAR_5981; -.
DR   KEGG; ocg:OCA5_c20430; -.
DR   PATRIC; fig|504832.7.peg.2163; -.
DR   eggNOG; COG0757; Bacteria.
DR   HOGENOM; CLU_090968_3_0_5; -.
DR   OMA; AYTHYSY; -.
DR   OrthoDB; 1872106at2; -.
DR   UniPathway; UPA00053; UER00086.
DR   Proteomes; UP000007730; Chromosome.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00466; DHQase_II; 1.
DR   Gene3D; 3.40.50.9100; -; 1.
DR   HAMAP; MF_00169; AroQ; 1.
DR   InterPro; IPR001874; DHquinase_II.
DR   InterPro; IPR018509; DHquinase_II_CS.
DR   InterPro; IPR036441; DHquinase_II_sf.
DR   PANTHER; PTHR21272; PTHR21272; 1.
DR   Pfam; PF01220; DHquinase_II; 1.
DR   PIRSF; PIRSF001399; DHquinase_II; 1.
DR   SUPFAM; SSF52304; SSF52304; 1.
DR   TIGRFAMs; TIGR01088; aroQ; 1.
DR   PROSITE; PS01029; DEHYDROQUINASE_II; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Reference proteome.
FT   CHAIN           1..151
FT                   /note="3-dehydroquinate dehydratase"
FT                   /id="PRO_1000097610"
FT   ACT_SITE        24
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   ACT_SITE        102
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         103..104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT   SITE            19
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
SQ   SEQUENCE   151 AA;  16248 MW;  55F942EECC2658CA CRC64;
     MTKTIYVLNG PNLNLLGTRE PDIYGHHTLA DVEALCRETA ARFGLEAVCH QTNREGEIVD
     LIHEAAKKQA AGLIINGGGY SHTSVAIHDA IVGVQIPTVE VHVSNVYARE RFRHQSFIAK
     AAFATLCGFG IEGYRLAILG LAARIGLAAK T